Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Modeling how many envelope glycoprotein trimers per virion participate in human immunodeficiency virus infectivity and its neutralization by antibody

8 Sept 2007

Abstract excerpt

No abstract is available from the source.

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Hepatitis C virus research
Share to HIV/AIDS drug development and treatment
Share to HIV Research and Treatment

Source

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Identifiers

PMID: 17825343
DOI: 10.1016/j.virol.2007.06.044

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 5 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Modeling how many envelope glycoprotein trimers per virion participate in human immunodeficiency virus infectivity and its neutralization by antibodyPMID 17825343Read ↗

Predicting HIV-1 transmission and antibody neutralization efficacy in vivo from stoichiometric parameters.Semantic proximity Read ↗

The HIV-1 envelope glycoprotein: structure, function and interactions with neutralizing antibodiesSemantic proximity Read ↗

Modeling coronavirus spike protein dynamics: implications for immunogenicity and immune escapeSemantic proximity Read ↗

Characterization of the Human Immunodeficiency Virus (HIV-1) Envelope Glycoprotein Conformational States on Infectious Virus ParticlesSemantic proximity Read ↗

Competitive assembly resolves the stoichiometry of essential proteins in infectious HIV-1 virionsSemantic proximity Read ↗

An all-atom view into the disordered interaction interface of the TRIM5 <i>α</i> PRYSPRY domain and the HIV capsidSemantic proximity Read ↗

Envelope Glycoprotein Trimers as HIV-1 Vaccine ImmunogensSemantic proximity Read ↗

Binding of inferred germline precursors of broadly neutralizing HIV-1 antibodies to native-like envelope trimersSemantic proximity Read ↗

Structural Rearrangements Maintain the Glycan Shield of an HIV-1 Envelope Trimer After the Loss of a GlycanSemantic proximity Read ↗

Mechanism for evolution of diverse autologous antibodies upon broadly neutralizing antibody therapy of people with HIVSemantic proximity Read ↗

Networks of HIV-1 Envelope Glycans Maintain Antibody Epitopes in the Face of Glycan Additions and Deletions.Semantic proximity Read ↗

HIV-1 Neutralization: Mechanisms and Relevance to Vaccine DesignSemantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.